Document Detail

Evidence for anion-translocating plant uncoupling mitochondrial protein in potato mitochondria.
MedLine Citation:
PMID:  8955108     Owner:  NLM     Status:  MEDLINE    
Transport properties of plant mitochondria from potato tubers were investigated using the swelling technique and membrane potential measurements. Proton-dependent swelling of fatty acid-depleted mitochondria in potassium acetate with valinomycin was possible only in the presence of fatty acids (linoleic acid and 12-(4-azido-2-nitrophenylamino)dodecanoic acid) and was inhibited by various purine nucleotides including ATP, GDP, and GTP. Swelling representing uptake of hexanesulfonate was also inhibited by purine nucleotides. Also, the membrane potential of fatty acid-depleted potato mitochondria energized by succinate declined upon the addition of linoleic acid or 12-(4-azido-2-nitrophenylamino)dodecanoic acid, and this decrease was prevented by ATP and other purine nucleotides. These transport activities are identical to those reported for brown adipose tissue mitochondria and related to the uncoupling protein; therefore, we ascribed them to the plant mitochondrial uncoupling protein (PUMP). A major difference between plant and mammalian uncoupling protein is that PUMP transports small hydrophilic anions such as Cl- very slowly, if at all. We suggest that PUMP may play an important role in plant physiology, where a regulated uncoupling and thermogenesis can proceed during fruit and seed development.
P Jezek; A D Costa; A E Vercesi
Related Documents :
8220238 - Pyridoxine is a precursor of the pyrimidine moiety of thiamin in saccharomyces cerevisiae.
22445368 - Polymorphism of the caprine malic enzyme 1 ( me1) gene and its association with milk qu...
10760258 - Peptide nucleic acids rather than rna may have been the first genetic molecule.
22630168 - Unexpected acidity enhancement triggered by alh3 association to phosphines.
23206858 - Comparative study of sulfite pretreatments for robust enzymatic saccharification of cor...
18648 - Studies on the inhibition of the desaturases by cyclopropenoid fatty acids.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  271     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1996 Dec 
Date Detail:
Created Date:  1997-01-23     Completed Date:  1997-01-23     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  32743-8     Citation Subset:  IM    
Department of Membrane Transport Biophysics, Institute of Physiology, Academy of Sciences, 14220 Prague 4, Czech Republic.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Alkanesulfonates / metabolism
Anions / metabolism
Biological Transport
Carrier Proteins / metabolism*
Chlorides / metabolism
Fatty Acids / metabolism
Hydrogen-Ion Concentration
Intracellular Membranes / physiology
Ion Channels
Membrane Potentials
Membrane Proteins / metabolism*
Mitochondria / metabolism*
Mitochondrial Proteins
Mitochondrial Swelling
Oxidative Phosphorylation
Solanum tuberosum / metabolism*
Uncoupling Agents
Reg. No./Substance:
0/Alkanesulfonates; 0/Anions; 0/Carrier Proteins; 0/Chlorides; 0/Fatty Acids; 0/Ion Channels; 0/Membrane Proteins; 0/Mitochondrial Proteins; 0/Uncoupling Agents; 0/mitochondrial uncoupling protein

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Cross-linking of engineered subunit delta to (alphabeta)3 in chloroplast F-ATPase.
Next Document:  Role of NHE3 in mediating renal brush border Na+-H+ exchange. Adaptation to metabolic acidosis.